\section{Conclusions}

%We presented a general overview of our protein unfolding experiments, and discussed the theory of Hyeon and Thirmulai that allows us to extract frustration energy scales from temperature dependent unfolding data.
%We also outlined the already completed temperature control module, and reviewed some previous frustration scale measurements in Ubiquitin.
%We gave a detailed report on the evolution and current status of the stepper motor control system and newtorked experiment server project, which are nearing completion.
%We presented some promising prelimary findings on our automatic force curve sorting algorithm.

We attempt to measure the free energy landscape roughness of protein molecules and to gain insight into the molecular mechanisms behind temperature changes in muscle stiffness.
To facilitate these measurements, software and hardware improvements to the experimental setup have been designed, constructed, and tested.
Specifically, the stepper motor has been automated, experiment server software has been written, and an automatic sorting algorithm is in development.

In the future, we hope to measure the frustration scale of the Titin domain I27, which will also server to stress-test the experiment server and sorting algorithm.
We also hope to add WLC fitting to our automatic curve sorter, removing as much subjectivity from our analysis as possible.
We will make a systematic study of the unfolding and refolding behaviors of I27 within the temperature range from 5{\dg}C to 50{\dg}C.
The results will be analyzed using the theory of Hyeon and Thirmulai.
Once the Titin measurements have been completed, our procedure should be stable enough for easy application to other proteins of interest, adding valuable information about the basic physics behind the protein folding problem.
